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Database: UniProt
Entry: A0A2A5W0D7_9BACT
LinkDB: A0A2A5W0D7_9BACT
Original site: A0A2A5W0D7_9BACT 
ID   A0A2A5W0D7_9BACT        Unreviewed;       105 AA.
AC   A0A2A5W0D7;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   24-JAN-2024, entry version 16.
DE   RecName: Full=Thioredoxin {ECO:0000256|PIRNR:PIRNR000077};
GN   Name=trxA {ECO:0000313|EMBL:PDH29960.1};
GN   ORFNames=CNC89_01860 {ECO:0000313|EMBL:PDH29960.1};
OS   Puniceicoccaceae bacterium MED-G31.
OC   Bacteria; Verrucomicrobiota; Opitutae; Puniceicoccales; Puniceicoccaceae.
OX   NCBI_TaxID=1986245 {ECO:0000313|EMBL:PDH29960.1, ECO:0000313|Proteomes:UP000219700};
RN   [1] {ECO:0000313|EMBL:PDH29960.1, ECO:0000313|Proteomes:UP000219700}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MED-G31 {ECO:0000313|EMBL:PDH29960.1};
RA   Haro-Moreno J.M., Lopez-Perez M., De La Torre J., Picazo A., Camacho A.,
RA   Rodriguez-Valera F.;
RT   "Fine stratification of microbial communities through a metagenomic profile
RT   of the photic zone.";
RL   Submitted (AUG-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the thioredoxin family.
CC       {ECO:0000256|ARBA:ARBA00008987, ECO:0000256|PIRNR:PIRNR000077}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:PDH29960.1}.
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DR   EMBL; NTJW01000007; PDH29960.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2A5W0D7; -.
DR   Proteomes; UP000219700; Unassembled WGS sequence.
DR   GO; GO:0015035; F:protein-disulfide reductase activity; IEA:InterPro.
DR   CDD; cd02947; TRX_family; 1.
DR   Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR   InterPro; IPR005746; Thioredoxin.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   InterPro; IPR017937; Thioredoxin_CS.
DR   InterPro; IPR013766; Thioredoxin_domain.
DR   NCBIfam; TIGR01068; thioredoxin; 1.
DR   PANTHER; PTHR45663; GEO12009P1; 1.
DR   PANTHER; PTHR45663:SF11; GEO12009P1; 1.
DR   Pfam; PF00085; Thioredoxin; 1.
DR   PIRSF; PIRSF000077; Thioredoxin; 1.
DR   PRINTS; PR00421; THIOREDOXIN.
DR   SUPFAM; SSF52833; Thioredoxin-like; 1.
DR   PROSITE; PS00194; THIOREDOXIN_1; 1.
DR   PROSITE; PS51352; THIOREDOXIN_2; 1.
PE   3: Inferred from homology;
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157,
KW   ECO:0000256|PIRSR:PIRSR000077-4};
KW   Electron transport {ECO:0000256|ARBA:ARBA00022982};
KW   Redox-active center {ECO:0000256|ARBA:ARBA00023284,
KW   ECO:0000256|PIRSR:PIRSR000077-4};
KW   Transport {ECO:0000256|ARBA:ARBA00022448}.
FT   DOMAIN          1..105
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000259|PROSITE:PS51352"
FT   ACT_SITE        33
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000077-1"
FT   ACT_SITE        36
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000077-1"
FT   SITE            27
FT                   /note="Deprotonates C-terminal active site Cys"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000077-1"
FT   SITE            34
FT                   /note="Contributes to redox potential value"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000077-1"
FT   SITE            35
FT                   /note="Contributes to redox potential value"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000077-1"
FT   DISULFID        33..36
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000077-4"
SQ   SEQUENCE   105 AA;  11497 MW;  4D5EC035B81BCBAE CRC64;
     MSENIIELDS SNFESTISDT SVPVVVDFWA PWCGPCKSIA PILEELASEL GESVKITKVN
     VDNNSEIATK YEIRAIPTIL VFRNGEIVET IVGLTSKDDL KAKLV
//
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